메뉴 건너뛰기




Volumn 1612, Issue 1, 2003, Pages 41-51

Effects of alterations of the amino-terminal glycine of influenza hemagglutinin fusion peptide on its structure, organization and membrane interactions

Author keywords

Amide proton exchange; Fluorescence quenching; Insertion angle; Insertion depth; Membrane fusion

Indexed keywords

DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; DODECYL SULFATE SODIUM; GLUTAMIC ACID; GLYCINE; HEMAGGLUTININ; LYSINE; SERINE;

EID: 0038702260     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(03)00084-1     Document Type: Article
Times cited : (21)

References (41)
  • 1
    • 0026492542 scopus 로고
    • Membrane fusion
    • White J.M. Membrane fusion. Science. 258:1992;917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 2
    • 0028298880 scopus 로고
    • Evidence for H(+)-induced insertion of influenza hemagglutinin HA2 N-terminal-segment into viral membrane
    • Weber T., Paesold G., Galli C., Mischler R., Semenza G., Brunner J. Evidence for H(+)-induced insertion of influenza hemagglutinin HA2 N-terminal-segment into viral membrane. J. Biol. Chem. 269:1994;18353-18358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18353-18358
    • Weber, T.1    Paesold, G.2    Galli, C.3    Mischler, R.4    Semenza, G.5    Brunner, J.6
  • 3
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton S.A., Calder L.J., Ruigrok R.W., Skehel J.J., Steinhauer D.A., Wiley D.C. Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J. 14:1995;240-246.
    • (1995) EMBO J. , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, L.J.2    Ruigrok, R.W.3    Skehel, J.J.4    Steinhauer, D.A.5    Wiley, D.C.6
  • 4
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer D.A., Wharton S.A., Skehel J.J., Wiley D.C. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:1995;6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 5
    • 0033539603 scopus 로고    scopus 로고
    • Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayer: Probing the role of hydrophobic residue size in the central region of the fusion peptide
    • Han X., Steinhauer D.A., Wharton S.A., Tamm L.K. Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayer: probing the role of hydrophobic residue size in the central region of the fusion peptide. Biochemistry. 38:1999;15052-15059.
    • (1999) Biochemistry , vol.38 , pp. 15052-15059
    • Han, X.1    Steinhauer, D.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 6
    • 0030012221 scopus 로고    scopus 로고
    • Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza fusion peptide with lipid bilayers
    • Gray C., Tatulian S.A., Wharton S.A., Tamm L.K. Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza fusion peptide with lipid bilayers. Biophys. J. 70:1996;2275-2286.
    • (1996) Biophys. J. , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 7
    • 0034705463 scopus 로고    scopus 로고
    • The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH
    • Chang D.K., Cheng S.F., Trivedi V.D., Yang S.H. The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. J. Biol. Chem. 275:2000;19150-19158.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19150-19158
    • Chang, D.K.1    Cheng, S.F.2    Trivedi, V.D.3    Yang, S.H.4
  • 8
    • 0035979369 scopus 로고    scopus 로고
    • Membrane interaction of mutated forms of the influenza peptide
    • Epand R.M., Epand R.F., Martin I., Ruysschaert J.M. Membrane interaction of mutated forms of the influenza peptide. Biochemistry. 40:2001;8800-8807.
    • (2001) Biochemistry , vol.40 , pp. 8800-8807
    • Epand, R.M.1    Epand, R.F.2    Martin, I.3    Ruysschaert, J.M.4
  • 9
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • Qiao H., Armstrong R.T., Melikyan G.B., Cohen F.S., White J.M. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol. Biol. Cell. 10:1999;2759-2769.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 10
    • 0035881708 scopus 로고    scopus 로고
    • Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    • Cross K.J., Wharton S.A., Skehel J.J., Wiley D.C., Steinhauer D.A. Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics. EMBO J. 20:2001;4432-4442.
    • (2001) EMBO J. , vol.20 , pp. 4432-4442
    • Cross, K.J.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Steinhauer, D.A.5
  • 11
    • 0026758174 scopus 로고
    • Aggregation and organization of pardaxin in phospholipid membranes
    • Ramalho-Santos J., Nir S., Duzgunes N., deCarvalho A.P., deLima M.daC. A common mechanism for influenza virus fusion activity and inactivation. Biochemistry. 23:1993;2279-2771.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6502-6509
    • Rapaport, D.1    Shai, Y.2
  • 13
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson W.C. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7:1990;205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 15
    • 0027240319 scopus 로고
    • Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study
    • Tamm L.K., Tatulian S.A. Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study. Biochemistry. 32:1993;7720-7726.
    • (1993) Biochemistry , vol.32 , pp. 7720-7726
    • Tamm, L.K.1    Tatulian, S.A.2
  • 16
    • 0343092088 scopus 로고    scopus 로고
    • Orientation of the infrared transition moments for an α-helix
    • Marsh D., Muller M., Schmitt F.J. Orientation of the infrared transition moments for an α-helix. Biophys. J. 78:2000;2499-2510.
    • (2000) Biophys. J. , vol.78 , pp. 2499-2510
    • Marsh, D.1    Muller, M.2    Schmitt, F.J.3
  • 18
    • 0030841309 scopus 로고    scopus 로고
    • The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface
    • Chang D.K., Cheng S.F., Chien W.J. The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface. J. Virol. 71:1997;6593-6602.
    • (1997) J. Virol. , vol.71 , pp. 6593-6602
    • Chang, D.K.1    Cheng, S.F.2    Chien, W.J.3
  • 19
    • 0019203091 scopus 로고
    • Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes
    • Maeda T., Ohnishi S. Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes. FEBS Lett. 122:1980;228-283.
    • (1980) FEBS Lett. , vol.122 , pp. 228-283
    • Maeda, T.1    Ohnishi, S.2
  • 20
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
    • Lear J.D., DeGrado W.F. Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2. J. Biol. Chem. 262:1987;6500-6505.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6500-6505
    • Lear, J.D.1    DeGrado, W.F.2
  • 23
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymer. 25:1986;469-487.
    • (1986) Biopolymer , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 24
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M., Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:1995;95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 25
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm L.K., Tatulian S.A. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30:1997;365-429.
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 26
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel β-helix proteins have a unique Fourier transform infrared spectrum?
    • Khurana R., Fink A.L. Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophys. J. 78:2000;994-1000.
    • (2000) Biophys. J. , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 27
    • 0027987329 scopus 로고
    • Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: A reexamination
    • Lewis R.N.A.H., McElhaney R.N., Pohle W., Mantsch H.H. Components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: a reexamination. Biophys. J. 67:1994;2367-2375.
    • (1994) Biophys. J. , vol.67 , pp. 2367-2375
    • Lewis, R.N.A.H.1    McElhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 28
    • 0035582246 scopus 로고    scopus 로고
    • Conformation and interaction with the membrane models of the amino-terminal peptide of influenza virus hemagglutinin HA2 at fusion pH
    • Chang D.K., Cheng S.F., Trivedi V.D. Conformation and interaction with the membrane models of the amino-terminal peptide of influenza virus hemagglutinin HA2 at fusion pH. Arch. Biochem. Biophys. 396:2001;89-98.
    • (2001) Arch. Biochem. Biophys. , vol.396 , pp. 89-98
    • Chang, D.K.1    Cheng, S.F.2    Trivedi, V.D.3
  • 29
    • 0035814820 scopus 로고    scopus 로고
    • Participation of two fusion peptides in measles virus-induced membrane fusion: Emerging similarity with other paramyxoviruses
    • Samuel O., Shai Y. Participation of two fusion peptides in measles virus-induced membrane fusion: emerging similarity with other paramyxoviruses. Biochemistry. 40:2001;1340-1349.
    • (2001) Biochemistry , vol.40 , pp. 1340-1349
    • Samuel, O.1    Shai, Y.2
  • 31
    • 0034091871 scopus 로고    scopus 로고
    • Tilted peptides: A motif for membrane destabilization (hypothesis)
    • Brasseur R. Tilted peptides: a motif for membrane destabilization (hypothesis). Mol. Membr. Biol. 17:2000;31-40.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 31-40
    • Brasseur, R.1
  • 32
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian S.A., Hinterdorfer P., Baber G., Tamm L.K. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14:1995;5514-5523.
    • (1995) EMBO J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 33
    • 0034671359 scopus 로고    scopus 로고
    • PH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers
    • Han X., Tamm L.K. pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers. J. Mol. Biol. 304:2000;953-965.
    • (2000) J. Mol. Biol. , vol.304 , pp. 953-965
    • Han, X.1    Tamm, L.K.2
  • 34
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformation change of the fusion domain from influenza hemagglutinin
    • Han X., Bushweller J.H., Cafiso D.S., Tamm L.K. Membrane structure and fusion-triggering conformation change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8:2001;715-721.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-721
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 35
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin
    • Doms R.W., Helenius A., White J. Membrane fusion activity of the influenza virus hemagglutinin. J. Biol. Chem. 260:1986;2973-2981.
    • (1986) J. Biol. Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 36
    • 0028023386 scopus 로고
    • Relation between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers
    • Epand R.M., Epand R.F. Relation between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochem. Biophys. Res. Commun. 202:1994;1420-1425.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1420-1425
    • Epand, R.M.1    Epand, R.F.2
  • 37
    • 0028840940 scopus 로고
    • Structure and topology of the influenza virus fusion peptide in lipid bilayers
    • Lüneberg J., Martin I., Nüßler F., Ruysschaert J.M., Herrmann A. Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:1995;27606-27614.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27606-27614
    • Lüneberg, J.1    Martin, I.2    Nüßler, F.3    Ruysschaert, J.M.4    Herrmann, A.5
  • 39
    • 0037869962 scopus 로고    scopus 로고
    • Lipid headgroup and peptide penetration, but not peptide oligomerization, modulate peptide-induced fusion
    • Pécheur E.I., Sainte-Marie J., Bienvenüe A., Hoekstra D. Lipid headgroup and peptide penetration, but not peptide oligomerization, modulate peptide-induced fusion. Biochemistry. 38:1999;364-373.
    • (1999) Biochemistry , vol.38 , pp. 364-373
    • Pécheur, E.I.1    Sainte-Marie, J.2    Bienvenüe, A.3    Hoekstra, D.4
  • 40
    • 0031012628 scopus 로고    scopus 로고
    • An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids
    • Chernomordik L.V., Leikina E., Frolov V., Bronk P., Zimmerberg J. An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids. J. Cell Biol. 136:1997;81-94.
    • (1997) J. Cell Biol. , vol.136 , pp. 81-94
    • Chernomordik, L.V.1    Leikina, E.2    Frolov, V.3    Bronk, P.4    Zimmerberg, J.5
  • 41
    • 0024593362 scopus 로고
    • Membrane fusion activity of influenza virus: Effects of gangliosides and negatively charged phospholipids in target liposomes
    • Stegmann T., Nir S., Wilschut J. Membrane fusion activity of influenza virus: effects of gangliosides and negatively charged phospholipids in target liposomes. Biochemistry. 28:1989;1698-1704.
    • (1989) Biochemistry , vol.28 , pp. 1698-1704
    • Stegmann, T.1    Nir, S.2    Wilschut, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.